ID A0A1M6CAA6_9BACT Unreviewed; 341 AA.
AC A0A1M6CAA6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065};
DE EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02065};
DE AltName: Full=Peptidoglycan polymerization terminase {ECO:0000256|HAMAP-Rule:MF_02065};
GN Name=mltG {ECO:0000256|HAMAP-Rule:MF_02065};
GN ORFNames=SAMN02745146_1088 {ECO:0000313|EMBL:SHI57949.1};
OS Hymenobacter daecheongensis DSM 21074.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1121955 {ECO:0000313|EMBL:SHI57949.1, ECO:0000313|Proteomes:UP000184418};
RN [1] {ECO:0000313|EMBL:SHI57949.1, ECO:0000313|Proteomes:UP000184418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21074 {ECO:0000313|EMBL:SHI57949.1,
RC ECO:0000313|Proteomes:UP000184418};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC peptidoglycan strands endolytically to terminate their elongation.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
CC -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; FQYN01000002; SHI57949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6CAA6; -.
DR STRING; 1121955.SAMN02745146_1088; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000184418; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1.
DR HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
DR NCBIfam; TIGR00247; endolytic transglycosylase MltG; 1.
DR PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30518; UNCHARACTERIZED; 1.
DR Pfam; PF02618; YceG; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02065};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02065};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02065};
KW Reference proteome {ECO:0000313|Proteomes:UP000184418};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02065};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02065}.
FT SITE 216
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 341 AA; 38799 MW; 70401E8209938388 CRC64;
MTGILLLLAL LLGGAALYAA WRVLWKPNVA VSAFGPAYLY IRTGAPYQAV LDSLERHELL
LEPETFRWLA ARRGYPARVR PGRYLLTPEL GNAALLERLT QGLQDTVHFE LNAFKYKPQL
VRQVSGQLEA DSGTLRRLLN DNTFLRRTYQ LDTTTILTLF LPGPYRLHWN TSARQFLDSA
AATHGRFWNA QRRQRADSLG LSPVQVHVLA SIVQRETAKP EDKPLIAGVY LNRLRHNMRL
QADPTLLWAI GNFGVRRVLN RDKLTDSPYN TYKHKGLPPG PITSANRQSL NAVLKPAAHK
FYFFCARPDL SGYSDFAETY AAHKRNARRY QHTLDSLKIR R
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